6W6E
The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined ClpB middle domain and a DnaK nucleotide binding domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0009408 | biological_process | response to heat |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0042026 | biological_process | protein refolding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0009408 | biological_process | response to heat |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0042026 | biological_process | protein refolding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0009408 | biological_process | response to heat |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0042026 | biological_process | protein refolding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0009408 | biological_process | response to heat |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0034605 | biological_process | cellular response to heat |
| D | 0042026 | biological_process | protein refolding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0009274 | cellular_component | peptidoglycan-based cell wall |
| E | 0009408 | biological_process | response to heat |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0034605 | biological_process | cellular response to heat |
| E | 0042026 | biological_process | protein refolding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0009274 | cellular_component | peptidoglycan-based cell wall |
| F | 0009408 | biological_process | response to heat |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0034605 | biological_process | cellular response to heat |
| F | 0042026 | biological_process | protein refolding |
| I | 0001968 | molecular_function | fibronectin binding |
| I | 0005524 | molecular_function | ATP binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0006457 | biological_process | protein folding |
| I | 0009274 | cellular_component | peptidoglycan-based cell wall |
| I | 0009408 | biological_process | response to heat |
| I | 0009986 | cellular_component | cell surface |
| I | 0010756 | biological_process | positive regulation of plasminogen activation |
| I | 0016887 | molecular_function | ATP hydrolysis activity |
| I | 0031072 | molecular_function | heat shock protein binding |
| I | 0035375 | molecular_function | zymogen binding |
| I | 0042026 | biological_process | protein refolding |
| I | 0042603 | cellular_component | capsule |
| I | 0044183 | molecular_function | protein folding chaperone |
| I | 0044406 | biological_process | adhesion of symbiont to host |
| I | 0046677 | biological_process | response to antibiotic |
| I | 0046688 | biological_process | response to copper ion |
| I | 0046777 | biological_process | protein autophosphorylation |
| I | 0051082 | molecular_function | unfolded protein binding |
| I | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
| I | 0071451 | biological_process | cellular response to superoxide |
| I | 0097691 | cellular_component | bacterial extracellular vesicle |
| I | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| I | 2000679 | biological_process | positive regulation of transcription regulatory region DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue AGS A 901 |
| Chain | Residue |
| A | PRO179 |
| A | LEU354 |
| A | PRO388 |
| B | ALA329 |
| B | ARG332 |
| B | ARG333 |
| A | VAL180 |
| A | ILE181 |
| A | ARG183 |
| A | GLY209 |
| A | GLY211 |
| A | LYS212 |
| A | THR213 |
| A | ILE350 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue AGS A 902 |
| Chain | Residue |
| A | ARG571 |
| A | THR609 |
| A | GLY610 |
| A | VAL611 |
| A | GLY612 |
| A | LYS613 |
| A | THR614 |
| A | GLU615 |
| A | GLN768 |
| A | ARG805 |
| A | ARG808 |
| B | ARG746 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue AGS B 901 |
| Chain | Residue |
| B | PRO179 |
| B | ILE181 |
| B | GLY209 |
| B | GLY211 |
| B | LYS212 |
| B | THR213 |
| B | LEU354 |
| C | ALA329 |
| C | ARG332 |
| C | ARG333 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue AGS B 902 |
| Chain | Residue |
| B | ARG571 |
| B | ILE573 |
| B | THR609 |
| B | GLY610 |
| B | VAL611 |
| B | GLY612 |
| B | LYS613 |
| B | THR614 |
| B | GLU615 |
| B | GLU680 |
| B | GLN768 |
| B | ALA804 |
| B | ARG805 |
| B | ARG808 |
| C | ARG746 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue AGS C 901 |
| Chain | Residue |
| C | ARG571 |
| C | VAL572 |
| C | ILE573 |
| C | THR609 |
| C | GLY610 |
| C | VAL611 |
| C | GLY612 |
| C | LYS613 |
| C | THR614 |
| C | GLU615 |
| C | ASN721 |
| C | GLN768 |
| C | ARG805 |
| C | ARG808 |
| D | GLU742 |
| D | ARG746 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue AGS D 901 |
| Chain | Residue |
| C | PRO179 |
| C | VAL180 |
| C | ILE181 |
| C | GLY209 |
| C | GLY211 |
| C | LYS212 |
| C | THR213 |
| C | ILE350 |
| C | LEU354 |
| D | ARG332 |
| D | ARG333 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue AGS D 902 |
| Chain | Residue |
| D | VAL180 |
| D | ILE181 |
| D | GLY209 |
| D | GLY211 |
| D | LYS212 |
| D | THR213 |
| D | ILE350 |
| D | LEU354 |
| E | ARG332 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue AGS D 903 |
| Chain | Residue |
| D | ARG808 |
| D | ARG571 |
| D | VAL572 |
| D | ILE573 |
| D | GLY574 |
| D | THR609 |
| D | GLY610 |
| D | VAL611 |
| D | GLY612 |
| D | LYS613 |
| D | THR614 |
| D | GLU615 |
| D | ALA804 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue AGS E 901 |
| Chain | Residue |
| E | ASP178 |
| E | PRO179 |
| E | VAL180 |
| E | PRO208 |
| E | GLY209 |
| E | VAL210 |
| E | GLY211 |
| E | LYS212 |
| E | THR213 |
| E | ALA214 |
| E | ILE350 |
| E | PRO388 |
| E | ASP389 |
| F | ARG332 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue ADP E 902 |
| Chain | Residue |
| E | ARG571 |
| E | VAL572 |
| E | ILE573 |
| E | THR609 |
| E | GLY610 |
| E | VAL611 |
| E | GLY612 |
| E | LYS613 |
| E | THR614 |
| E | ILE764 |
| E | ALA804 |
| E | ARG805 |
| site_id | AD2 |
| Number of Residues | 15 |
| Details | binding site for residue AGS F 901 |
| Chain | Residue |
| A | ARG746 |
| F | ARG571 |
| F | VAL572 |
| F | ILE573 |
| F | THR609 |
| F | GLY610 |
| F | VAL611 |
| F | GLY612 |
| F | LYS613 |
| F | THR614 |
| F | GLU615 |
| F | ILE764 |
| F | ALA804 |
| F | ARG805 |
| F | ARG808 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue ADP F 902 |
| Chain | Residue |
| F | ASP178 |
| F | PRO179 |
| F | GLU207 |
| F | PRO208 |
| F | GLY209 |
| F | VAL210 |
| F | GLY211 |
| F | LYS212 |
| F | THR213 |
| F | ALA214 |
| F | ILE350 |
| F | LEU354 |
Functional Information from PROSITE/UniProt
| site_id | PS00297 |
| Number of Residues | 8 |
| Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS |
| Chain | Residue | Details |
| I | ILE7-SER14 |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL |
| Chain | Residue | Details |
| I | VAL168-LEU181 |
| site_id | PS00870 |
| Number of Residues | 13 |
| Details | CLPAB_1 Chaperonins clpA/B signature 1. DAGNMIKPmLarG |
| Chain | Residue | Details |
| A | ASP295-GLY307 |
| site_id | PS00871 |
| Number of Residues | 19 |
| Details | CLPAB_2 Chaperonins clpA/B signature 2. RIDmSEYgEKhTvARLiGA |
| Chain | Residue | Details |
| A | ARG633-ALA651 |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. VvLvGGsTRMPaVtD |
| Chain | Residue | Details |
| I | VAL310-ASP324 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250 |
| Chain | Residue | Details |
| I | THR175 | |
| E | GLY607 | |
| F | GLY206 | |
| F | GLY607 | |
| A | GLY607 | |
| B | GLY206 | |
| B | GLY607 | |
| C | GLY206 | |
| C | GLY607 | |
| D | GLY206 | |
| D | GLY607 | |
| E | GLY206 |
